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Volumn 516, Issue , 2002, Pages 99-118

The molecular basis of Friedreich ataxia

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; DEFEROXAMINE; FRATAXIN; IRON; UBIQUINONE DERIVATIVE;

EID: 0036940427     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4615-0117-6_5     Document Type: Review
Times cited : (42)

References (105)
  • 1
    • 0017056474 scopus 로고
    • Clinical description and roentgenologic evaluation of patients with Friedreich ataxia
    • Geoffroy G, Barbeau A, Breton, G et al. Clinical description and roentgenologic evaluation of patients with Friedreich ataxia. Can J Neurol Sci 1976; 3:279-286.
    • (1976) Can J Neurol Sci , vol.3 , pp. 279-286
    • Geoffroy, G.1    Barbeau, A.2    Breton, G.3
  • 2
    • 0019782799 scopus 로고
    • Friedreich ataxia: A clinical and genetic study of 90 families with an analysis of early diagnosis criteria and intrafamilial clustering of clinical features
    • Harding AE. Friedreich ataxia: A clinical and genetic study of 90 families with an analysis of early diagnosis criteria and intrafamilial clustering of clinical features. Brain 1981; 104:589-620.
    • (1981) Brain , vol.104 , pp. 589-620
    • Harding, A.E.1
  • 3
    • 0002654217 scopus 로고    scopus 로고
    • The neuropathology of inherited ataxias
    • Manto M, Pandolfo M, eds. Cambridge: Cambridge University Press: Part VII, Neuropathology
    • Koeppen A. The neuropathology of inherited ataxias. In: Manto M, Pandolfo M, eds. The Cerebellum and its Disorders. Cambridge: Cambridge University Press, 2001: Part VII, Neuropathology: 25.
    • (2001) The Cerebellum and its Disorders , pp. 25
    • Koeppen, A.1
  • 4
    • 13344270899 scopus 로고    scopus 로고
    • Friedreich ataxia: Autosomal recessive disease caused by an intronic GAA triplet repeat expansion
    • Campuzano V, Montermini L, Moltȯ MD, Pianese L, Cossée M, Cavalcanti F et al. Friedreich ataxia: Autosomal recessive disease caused by an intronic GAA triplet repeat expansion. Science 1996; 271:1423-1427.
    • (1996) Science , vol.271 , pp. 1423-1427
    • Campuzano, V.1    Montermini, L.2    Molto, M.D.3    Pianese, L.4    Cossée, M.5    Cavalcanti, F.6
  • 5
    • 17144467700 scopus 로고    scopus 로고
    • Phenotypic variability in Friedreich ataxia: Role of the associated GAA triplet repeat expansion
    • Montermini L, Richter A, Morgan K, Justice CM, Julien D, Castelloti B et al. Phenotypic variability in Friedreich ataxia: role of the associated GAA triplet repeat expansion. Ann Neurol 1997; 41:675-682.
    • (1997) Ann Neurol , vol.41 , pp. 675-682
    • Montermini, L.1    Richter, A.2    Morgan, K.3    Justice, C.M.4    Julien, D.5    Castelloti, B.6
  • 6
    • 0023751357 scopus 로고
    • Mapping of mutation causing Friedreich' ataxia to human chromosome 9
    • Chamberlain S, Shaw J, Rowland A et al. Mapping of mutation causing Friedreich' ataxia to human chromosome 9. Nature 1988; 334:248-250.
    • (1988) Nature , vol.334 , pp. 248-250
    • Chamberlain, S.1    Shaw, J.2    Rowland, A.3
  • 7
    • 0030826433 scopus 로고    scopus 로고
    • Frataxin shows developmentally regulated tissue-specific expression in the mouse embryo
    • Jiralerspong S, Liu Y, Montermini L, Stifani S, Pandolfo M. Frataxin shows developmentally regulated tissue-specific expression in the mouse embryo. Neurobiol Dis 1997; 4:103-113.
    • (1997) Neurobiol Dis , vol.4 , pp. 103-113
    • Jiralerspong, S.1    Liu, Y.2    Montermini, L.3    Stifani, S.4    Pandolfo, M.5
  • 8
    • 0030813487 scopus 로고    scopus 로고
    • Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin
    • Koutnikova H, Campuzano V, Foury F, Dollé P, Cazzalini O, Koenig M. Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin. Nat Genet 1997; 16:345-351.
    • (1997) Nat Genet , vol.16 , pp. 345-351
    • Koutnikova, H.1    Campuzano, V.2    Foury, F.3    Dollé, P.4    Cazzalini, O.5    Koenig, M.6
  • 9
    • 0030739437 scopus 로고    scopus 로고
    • Evolution of the Friedreich ataxia trinucleotide repeat expansion: Founder effect and premutations
    • Cossée M, Schmitt M, Campuzano V et al. Evolution of the Friedreich ataxia trinucleotide repeat expansion: Founder effect and premutations. Proc Natl Acad Sci USA 1997; 94:7452-7457.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7452-7457
    • Cossée, M.1    Schmitt, M.2    Campuzano, V.3
  • 10
    • 8544240144 scopus 로고    scopus 로고
    • The Friedreich ataxia GAA triplet repeat: Premutation and normal alleles
    • Montermini L, Andermann E, Labuda M et al. The Friedreich ataxia GAA triplet repeat: premutation and normal alleles. Hum Mol Genet 1997; 6:1261-1266.
    • (1997) Hum Mol Genet , vol.6 , pp. 1261-1266
    • Montermini, L.1    Andermann, E.2    Labuda, M.3
  • 11
    • 0344820730 scopus 로고    scopus 로고
    • Frataxin point mutations and clinical presentation of compound heterozygous Friedreich ataxia patients
    • Cossée M, Dürr A, Schmitt M et al. Frataxin point mutations and clinical presentation of compound heterozygous Friedreich ataxia patients. Ann Neurol 1999; 45:200-206.
    • (1999) Ann Neurol , vol.45 , pp. 200-206
    • Cossée, M.1    Dürr, A.2    Schmitt, M.3
  • 12
    • 0029821176 scopus 로고    scopus 로고
    • Clinical and genetic abnormalities in patients with Friedreich ataxia
    • Dürr A, Cossée M, Agid Y et al. Clinical and genetic abnormalities in patients with Friedreich ataxia. N Engl J Med 1996; 335:1169-1175.
    • (1996) N Engl J Med , vol.335 , pp. 1169-1175
    • Dürr, A.1    Cossée, M.2    Agid, Y.3
  • 13
    • 0029757676 scopus 로고    scopus 로고
    • The relationship between trinucleotide (GAA) repeat length and clinical features in Friedreich ataxia
    • Filla A, De Michele G, Cavalcanti F et al. The relationship between trinucleotide (GAA) repeat length and clinical features in Friedreich ataxia. Am J Hum Genet 1996; 59:554-560.
    • (1996) Am J Hum Genet , vol.59 , pp. 554-560
    • Filla, A.1    De Michele, G.2    Cavalcanti, F.3
  • 15
    • 0030862745 scopus 로고    scopus 로고
    • Phenotype correlation and intergenerational dynamics of the Friedreich ataxia GAA trinucleotide repeat
    • Monros E, Moltó MD, Martinez F et al. Phenotype correlation and intergenerational dynamics of the Friedreich ataxia GAA trinucleotide repeat. Am J Hum Genet 1997; 61:101-110.
    • (1997) Am J Hum Genet , vol.61 , pp. 101-110
    • Monros, E.1    Moltó, M.D.2    Martinez, F.3
  • 16
    • 0030815628 scopus 로고    scopus 로고
    • Somatic mosaicism for the Friedreich's ataxia GAA triplet repeat expansions in the central nervous system
    • Montermini L, Kish SJ, Jiralerspong S, Lamarche JB, Pandolfo M. Somatic mosaicism for the Friedreich's ataxia GAA triplet repeat expansions in the central nervous system. Neurology 1997; 49:606-610.
    • (1997) Neurology , vol.49 , pp. 606-610
    • Montermini, L.1    Kish, S.J.2    Jiralerspong, S.3    Lamarche, J.B.4    Pandolfo, M.5
  • 17
    • 0030045979 scopus 로고    scopus 로고
    • The age of Alu subfamilies
    • Kapitonov V, Jurka J. The age of Alu subfamilies. J Mol Evol 1996; 42:59-65.
    • (1996) J Mol Evol , vol.42 , pp. 59-65
    • Kapitonov, V.1    Jurka, J.2
  • 19
    • 0028242797 scopus 로고
    • Simple repeat DNA is not replicated simply
    • Richards RI, Sutherland GR. Simple repeat DNA is not replicated simply. Nature Genet 1994; 6:114-116.
    • (1994) Nature Genet , vol.6 , pp. 114-116
    • Richards, R.I.1    Sutherland, G.R.2
  • 20
    • 0030058075 scopus 로고    scopus 로고
    • Molecular basis of genetic instability of triplet repeats
    • Wells RD. Molecular basis of genetic instability of triplet repeats. J Biol Chem 1996; 271:2875-2878.
    • (1996) J Biol Chem , vol.271 , pp. 2875-2878
    • Wells, R.D.1
  • 21
    • 0034665718 scopus 로고    scopus 로고
    • Tandem duplication. A novel type of triplet repeat instability
    • Pluciennik A, Iyer RR, Parniewski P, Wells RD. Tandem duplication. A novel type of triplet repeat instability. J Biol Chem 2000; 275:28386-28397.
    • (2000) J Biol Chem , vol.275 , pp. 28386-28397
    • Pluciennik, A.1    Iyer, R.R.2    Parniewski, P.3    Wells, R.D.4
  • 22
    • 0034704123 scopus 로고    scopus 로고
    • Gene conversion (recombination) mediates expansions of CTG•CAG repeats
    • Jakupciak JP, Wells RD. Gene conversion (recombination) mediates expansions of CTG•CAG repeats. J Biol Chem 2000; 275:40003-40013.
    • (2000) J Biol Chem , vol.275 , pp. 40003-40013
    • Jakupciak, J.P.1    Wells, R.D.2
  • 23
    • 0030809774 scopus 로고    scopus 로고
    • The genetic clock and the age of the founder effect in growing populations: A lesson from French Canadians and Ashkenazim
    • Labuda D, Labuda M, Zietkiewicz E. The genetic clock and the age of the founder effect in growing populations: a lesson from French Canadians and Ashkenazim. Am J Hum Genet 1997; 61:768-771.
    • (1997) Am J Hum Genet , vol.61 , pp. 768-771
    • Labuda, D.1    Labuda, M.2    Zietkiewicz, E.3
  • 25
    • 0034720861 scopus 로고    scopus 로고
    • Unique origin and specific ethnic distribution of the Friedreich ataxia GAA expansion
    • Labuda M, Labuda D, Miranda C, Poirier J, Soong B, Barucha NE et al. Unique origin and specific ethnic distribution of the Friedreich ataxia GAA expansion. Neurology 2000; 54:2322-2324.
    • (2000) Neurology , vol.54 , pp. 2322-2324
    • Labuda, M.1    Labuda, D.2    Miranda, C.3    Poirier, J.4    Soong, B.5    Barucha, N.E.6
  • 26
    • 0030724120 scopus 로고    scopus 로고
    • The Friedreich's Ataxia GAA repeat expansion in patients with recessive or sporadic ataxia
    • Geschwind DH, Perlman S, Grody W et al. The Friedreich's Ataxia GAA repeat expansion in patients with recessive or sporadic ataxia. Neurology 1997; 49:1004-1009.
    • (1997) Neurology , vol.49 , pp. 1004-1009
    • Geschwind, D.H.1    Perlman, S.2    Grody, W.3
  • 28
    • 0029053371 scopus 로고
    • Trinucleotide repeats that expand in human disease form hairpin structures in vitro
    • Gacy AM, Goellner G, Juranic N, Macura S, McMurray CT. Trinucleotide repeats that expand in human disease form hairpin structures in vitro. Cell 1995; 81:533-540.
    • (1995) Cell , vol.81 , pp. 533-540
    • Gacy, A.M.1    Goellner, G.2    Juranic, N.3    Macura, S.4    McMurray, C.T.5
  • 29
    • 0027475856 scopus 로고
    • Crystal structure of an oligonucleotide duplex containing G•G base pairs: Influence of mispairing on DNA backbone conformation
    • Skelly JV, Edwards KJ, Jenkins TC, Neidle S. Crystal structure of an oligonucleotide duplex containing G•G base pairs: Influence of mispairing on DNA backbone conformation. Proc Natl Acad Sci USA 1993; 90:804-808.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 804-808
    • Skelly, J.V.1    Edwards, K.J.2    Jenkins, T.C.3    Neidle, S.4
  • 30
    • 0023796273 scopus 로고
    • The chemistry and biology of unusual DNA structures adopted by oligopurine-oligopyrimidine sequences
    • Wells RD, Collier DA, Hanvey JC, Shimizu M, Wohlrab F. The chemistry and biology of unusual DNA structures adopted by oligopurine-oligopyrimidine sequences. FASEB J 1988; 2:2939-2949.
    • (1988) FASEB J , vol.2 , pp. 2939-2949
    • Wells, R.D.1    Collier, D.A.2    Hanvey, J.C.3    Shimizu, M.4    Wohlrab, F.5
  • 31
    • 0034612992 scopus 로고    scopus 로고
    • Unexpected formation of parallel duplex in GAA and TTC trinucleotide repeats of Friedreich's ataxia
    • LeProust EM, Pearso CE, Sinden RR, Gao X. Unexpected formation of parallel duplex in GAA and TTC trinucleotide repeats of Friedreich's ataxia. J Mol Biol 2000; 302:1063-1080.
    • (2000) J Mol Biol , vol.302 , pp. 1063-1080
    • LeProust, E.M.1    Pearso, C.E.2    Sinden, R.R.3    Gao, X.4
  • 32
  • 34
    • 0033544301 scopus 로고    scopus 로고
    • A nonpathogenic GAAGGA repeat in the Friedreich gene: Implications for pathogenesis
    • Ohshima K, Sakamoto N, Labuda M et al. A nonpathogenic GAAGGA repeat in the Friedreich gene: Implications for pathogenesis. Neurol 1999; 53:1854-1857
    • (1999) Neurol , vol.53 , pp. 1854-1857
    • Ohshima, K.1    Sakamoto, N.2    Labuda, M.3
  • 35
    • 0000221135 scopus 로고
    • Defined ordered sequence DNA, DNA structure, and DNA-directed mutation
    • Davies K, Warren S, eds. Cold Spring Harbor Press
    • Wells RD, Sinden RR. Defined ordered sequence DNA, DNA structure, and DNA-directed mutation. In: Davies K, Warren S, eds. Genome Analysis. Vol. 7. Genome Rearrangement and Stability. Cold Spring Harbor Press, 1993:107-138.
    • (1993) Genome Analysis. Vol. 7. Genome Rearrangement and Stability , vol.7 , pp. 107-138
    • Wells, R.D.1    Sinden, R.R.2
  • 40
    • 0028803597 scopus 로고
    • An intramolecular triplex in the human gamma-globin 5′-flanking region is altered by point mutations associated with hereditary persistence of fetal hemoglobin
    • Bacolla A, Ulrich MJ, Larson JE, Ley TJ, Wells RD. An intramolecular triplex in the human gamma-globin 5′-flanking region is altered by point mutations associated with hereditary persistence of fetal hemoglobin. J Biol Chem 1995; 270:24556-24563.
    • (1995) J Biol Chem , vol.270 , pp. 24556-24563
    • Bacolla, A.1    Ulrich, M.J.2    Larson, J.E.3    Ley, T.J.4    Wells, R.D.5
  • 41
    • 0030018680 scopus 로고    scopus 로고
    • Characterization of a polypyrimidine/polypurine tract in the promoter of the gene for chicken malic enzyme
    • Xu G, Goodridge AG. Characterization of a polypyrimidine/polypurine tract in the promoter of the gene for chicken malic enzyme. J Biol Chem 1996; 271:16008-16019.
    • (1996) J Biol Chem , vol.271 , pp. 16008-16019
    • Xu, G.1    Goodridge, A.G.2
  • 42
    • 0023891939 scopus 로고
    • Influence of DNA sequence on the formation of non-B right-handed helices in oligopurine/oligopyrimidine inserts in plasmids
    • Hanvey JC, Klysik J, Wells RD. Influence of DNA sequence on the formation of non-B right-handed helices in oligopurine/oligopyrimidine inserts in plasmids. J Biol Chem 1988; 263:7386-7396.
    • (1988) J Biol Chem , vol.263 , pp. 7386-7396
    • Hanvey, J.C.1    Klysik, J.2    Wells, R.D.3
  • 43
    • 0011204402 scopus 로고
    • Intramolecular DNA triplexes in supercoiled plasmids
    • Hanvey JC, Shimizu M, Wells RD. Intramolecular DNA triplexes in supercoiled plasmids. Proc Natl Acad Sci 1988; 85:6292-6296.
    • (1988) Proc Natl Acad Sci , vol.85 , pp. 6292-6296
    • Hanvey, J.C.1    Shimizu, M.2    Wells, R.D.3
  • 44
    • 0024598556 scopus 로고
    • Intramolecular DNA triplexes in supercoiled plasmids: I. Effect of loop size on formation and stability
    • Shimizu M, Hanvey JC, Wells RD. Intramolecular DNA triplexes in supercoiled plasmids: I. Effect of loop size on formation and stability. J Biol Chem 1989; 264:5944-5949.
    • (1989) J Biol Chem , vol.264 , pp. 5944-5949
    • Shimizu, M.1    Hanvey, J.C.2    Wells, R.D.3
  • 45
    • 0024600845 scopus 로고
    • Intramolecular DNA triplexes in supercoiled plasmids: II. Effect of base composition and non-central interruptions on formation and stability
    • Hanvey JC, Shimizu M, Wells RD. Intramolecular DNA triplexes in supercoiled plasmids: II. Effect of base composition and non-central interruptions on formation and stability. J Biol Chem 1989; 264:5950-5956.
    • (1989) J Biol Chem , vol.264 , pp. 5950-5956
    • Hanvey, J.C.1    Shimizu, M.2    Wells, R.D.3
  • 46
    • 0025058003 scopus 로고
    • Site-specific inhibition of EcoR1 restriction/modification enzymes via DNA triple helix
    • Hanvey JC, Shimizu M. Wells RD. Site-specific inhibition of EcoR1 restriction/modification enzymes via DNA triple helix. Nucl Acids Res 1989; 18:157-161.
    • (1989) Nucl Acids Res , vol.18 , pp. 157-161
    • Hanvey, J.C.1    Shimizu, M.2    Wells, R.D.3
  • 47
    • 0025301201 scopus 로고
    • Multiple Non-B-DNA Conformations of polypurine/polypyrimidine sequences in plasmids
    • Shimizu M, Hanvey JC, Wells RD. Multiple Non-B-DNA Conformations of polypurine/polypyrimidine sequences in plasmids. Biochemistry 1990; 29:4704-4713.
    • (1990) Biochemistry , vol.29 , pp. 4704-4713
    • Shimizu, M.1    Hanvey, J.C.2    Wells, R.D.3
  • 48
    • 0026570255 scopus 로고
    • Metal ions cause the isomerization of certain intramolecular triplexes
    • Kang S, Wohlrab F, Wells RD. Metal ions cause the isomerization of certain intramolecular triplexes. J Biol Chem 1992; 267:1259-1264.
    • (1992) J Biol Chem , vol.267 , pp. 1259-1264
    • Kang, S.1    Wohlrab, F.2    Wells, R.D.3
  • 49
    • 0026703204 scopus 로고
    • GC rich flanking tracts decrease the kinetics of intramolecular DNA triplex formation
    • Kang S, Wohlrab F, Wells RD. GC rich flanking tracts decrease the kinetics of intramolecular DNA triplex formation. J Biol Chem 1992; 267:19435-19442.
    • (1992) J Biol Chem , vol.267 , pp. 19435-19442
    • Kang, S.1    Wohlrab, F.2    Wells, R.D.3
  • 50
    • 0029950726 scopus 로고    scopus 로고
    • Cloning, characterization, and properties of seven triplet repeat DNA sequences
    • Ohshima K, Kang S, Larson JE, Wells RD. Cloning, characterization, and properties of seven triplet repeat DNA sequences. J Biol Chem 1996; 271:16773-16783.
    • (1996) J Biol Chem , vol.271 , pp. 16773-16783
    • Ohshima, K.1    Kang, S.2    Larson, J.E.3    Wells, R.D.4
  • 51
    • 0014414243 scopus 로고
    • Specificity of the three-stranded complex formation between double-stranded DNA and single-stranded RNA containing repeating nucleotide sequences
    • Morgan AR, Wells RD. Specificity of the three-stranded complex formation between double-stranded DNA and single-stranded RNA containing repeating nucleotide sequences. J Mol Biol 1968; 37:63-80.
    • (1968) J Mol Biol , vol.37 , pp. 63-80
    • Morgan, A.R.1    Wells, R.D.2
  • 52
    • 0025744428 scopus 로고
    • Evidence that a triplex-forming oligodeoxyribonucleotide binds to the c-myc promoter in HeLa cells, thereby reducing c-myc mRNA levels
    • Postel EH, Flint SJ, Kessler DJ, Hogan ME. Evidence that a triplex-forming oligodeoxyribonucleotide binds to the c-myc promoter in HeLa cells, thereby reducing c-myc mRNA levels. Proc Natl Acad Sci USA 1991; 88:8227-8231.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8227-8231
    • Postel, E.H.1    Flint, S.J.2    Kessler, D.J.3    Hogan, M.E.4
  • 54
    • 0022483582 scopus 로고
    • Hypotrophic and dying-back nerve fibers in Friedreich's ataxia
    • Said G, Marion MH, Selva J, Jamet C. Hypotrophic and dying-back nerve fibers in Friedreich's ataxia. Neurology 1986; 36:1292-1299.
    • (1986) Neurology , vol.36 , pp. 1292-1299
    • Said, G.1    Marion, M.H.2    Selva, J.3    Jamet, C.4
  • 56
    • 0028941326 scopus 로고    scopus 로고
    • Early-onset ataxia with cardiomyopathy and retained tendon reflexes maps to Friedreich's ataxia locus on chromosome 9q
    • Palau F, De Michele G, Vilchez JJ, Pandolfo M, Monros E, Cocozza S et al. Early-onset ataxia with cardiomyopathy and retained tendon reflexes maps to Friedreich's ataxia locus on chromosome 9q. Ann Neurol 1997; 37:359-362.
    • (1997) Ann Neurol , vol.37 , pp. 359-362
    • Palau, F.1    De Michele, G.2    Vilchez, J.J.3    Pandolfo, M.4    Monros, E.5    Cocozza, S.6
  • 58
    • 0024375758 scopus 로고
    • Preclinical and manifest diabetes mellitus in young patients with Friedreich's ataxia: No evidence of immune process behind the islet cell destruction
    • Schoenle EJ, Boltshauser EJ, Baekkeskov S, Landin Olsson M, Torresani T, von Felten A. Preclinical and manifest diabetes mellitus in young patients with Friedreich's ataxia: No evidence of immune process behind the islet cell destruction. Diabetologia 1989; 32:378-381.
    • (1989) Diabetologia , vol.32 , pp. 378-381
    • Schoenle, E.J.1    Boltshauser, E.J.2    Baekkeskov, S.3    Landin Olsson, M.4    Torresani, T.5    Von Felten, A.6
  • 59
    • 0027534291 scopus 로고
    • Evidence for abnormal regulation of insulin receptors in Friedreich's ataxia
    • Fantus IG, Seni MH, Andermann E. Evidence for abnormal regulation of insulin receptors in Friedreich's ataxia. J Clin Endocrinol Metab 1993; 76:60-63.
    • (1993) J Clin Endocrinol Metab , vol.76 , pp. 60-63
    • Fantus, I.G.1    Seni, M.H.2    Andermann, E.3
  • 61
    • 0031941447 scopus 로고    scopus 로고
    • The GAA triplet-repeat expansion in Friedreich's ataxia interferes with transcription and may be associated with an unusual DNA structure
    • Bidichandani SI, Ashizawa T, Patel PI. The GAA triplet-repeat expansion in Friedreich's ataxia interferes with transcription and may be associated with an unusual DNA structure. Am J Hum Genet 1998; 62:111-121.
    • (1998) Am J Hum Genet , vol.62 , pp. 111-121
    • Bidichandani, S.I.1    Ashizawa, T.2    Patel, P.I.3
  • 62
    • 0029757676 scopus 로고    scopus 로고
    • The relationship between trinucleotide (GAA) repeat length and clinical features in Friedreich ataxia
    • Filla A, De Michele G, Cavalcanti F, Pianese L, Monticelli A, Campanella G et al. The relationship between trinucleotide (GAA) repeat length and clinical features in Friedreich ataxia. Am J Hum Genet 1996; 59:554-560.
    • (1996) Am J Hum Genet , vol.59 , pp. 554-560
    • Filla, A.1    De Michele, G.2    Cavalcanti, F.3    Pianese, L.4    Monticelli, A.5    Campanella, G.6
  • 63
    • 0032486276 scopus 로고    scopus 로고
    • Inhibitory effects of expanded GAA•TTC triplet repeats from intron 1 of Friedreich's ataxia gene on transcription and replication in vivo
    • Ohshima K, Montermini L, Wells RD, Pandolfo M. Inhibitory effects of expanded GAA•TTC triplet repeats from intron 1 of Friedreich's ataxia gene on transcription and replication in vivo. J Biol Chem 1998; 273:14588-14595.
    • (1998) J Biol Chem , vol.273 , pp. 14588-14595
    • Ohshima, K.1    Montermini, L.2    Wells, R.D.3    Pandolfo, M.4
  • 66
    • 0025225502 scopus 로고
    • Induction of RNA-stabilized DNA conformers by transcription of an immunoglobulin switch region
    • Reaban ME, Griffin JA. Induction of RNA-stabilized DNA conformers by transcription of an immunoglobulin switch region. Nature 1990; 348:342-344.
    • (1990) Nature , vol.348 , pp. 342-344
    • Reaban, M.E.1    Griffin, J.A.2
  • 67
    • 0012361877 scopus 로고
    • Scientific correspondence
    • Reaban ME, Griffin JA. Scientific correspondence. Nature 1991; 351:447-448.
    • (1991) Nature , vol.351 , pp. 447-448
    • Reaban, M.E.1    Griffin, J.A.2
  • 68
    • 0028106344 scopus 로고
    • Transcription induces the formation of a stable RNA.DNA hybrid in the immunoglobulin alpha switch region
    • Reaban ME, Lebowitz J, Griffin JA. Transcription induces the formation of a stable RNA.DNA hybrid in the immunoglobulin alpha switch region. J Biol Chem 1994; 269:21850-21857.
    • (1994) J Biol Chem , vol.269 , pp. 21850-21857
    • Reaban, M.E.1    Lebowitz, J.2    Griffin, J.A.3
  • 69
    • 0028929024 scopus 로고
    • A long purine-pyrimidine homopolymer acts as a transriptional diode
    • Grabczyk E, Fishman MC. A long purine-pyrimidine homopolymer acts as a transriptional diode. J Biol Chem 1995; 270:1791-1797.
    • (1995) J Biol Chem , vol.270 , pp. 1791-1797
    • Grabczyk, E.1    Fishman, M.C.2
  • 70
    • 9844222853 scopus 로고    scopus 로고
    • Frataxin is reduced in Friedreich ataxia patients and is associated with mitochondrial membranes
    • Campuzano V, Montermini L, Lutz Y et al. Frataxin is reduced in Friedreich ataxia patients and is associated with mitochondrial membranes. Hum Mol Genet 1997; 6:1771-1780.
    • (1997) Hum Mol Genet , vol.6 , pp. 1771-1780
    • Campuzano, V.1    Montermini, L.2    Lutz, Y.3
  • 72
    • 0030862745 scopus 로고    scopus 로고
    • Phenotype correlation and intergenerational dynamics of the Friedreich ataxia GAA trinucleotide repeat
    • Monros E, Moltó MD, Martinez F et al. Phenotype correlation and intergenerational dynamics of the Friedreich ataxia GAA trinucleotide repeat. Am J Hum Genet 1997; 61:101-110.
    • (1997) Am J Hum Genet , vol.61 , pp. 101-110
    • Monros, E.1    Moltó, M.D.2    Martinez, F.3
  • 73
    • 0030904035 scopus 로고    scopus 로고
    • Identification and sizing of the GAA trinucleotide repeat expansion of Friedreich ataxia in 56 patients - Clinical and genetic correlates
    • Lamont PJ, Davis MB, Wood NW. Identification and sizing of the GAA trinucleotide repeat expansion of Friedreich ataxia in 56 patients - Clinical and genetic correlates. Brain 1997; 120:673-680.
    • (1997) Brain , vol.120 , pp. 673-680
    • Lamont, P.J.1    Davis, M.B.2    Wood, N.W.3
  • 74
    • 1842370633 scopus 로고    scopus 로고
    • Friedreich ataxia. Revision of the phenotype according to molecular genetics
    • Schols L, Amoiridis G, Przuntek H, Frank G, Epplen JT, Epplen C. Friedreich ataxia. Revision of the phenotype according to molecular genetics. Brain 1997; 120:2131-2140.
    • (1997) Brain , vol.120 , pp. 2131-2140
    • Schols, L.1    Amoiridis, G.2    Przuntek, H.3    Frank, G.4    Epplen, J.T.5    Epplen, C.6
  • 75
    • 0030895266 scopus 로고    scopus 로고
    • Atypical Friedreich ataxia caused by compound heterozygosity for a novel missense mutation and the GAA triplet-repeat expansion
    • Bidichandani SI, Ashizawa T, Patel PI. Atypical Friedreich ataxia caused by compound heterozygosity for a novel missense mutation and the GAA triplet-repeat expansion. Am J Hum Genet 1997; 60:1251-1256.
    • (1997) Am J Hum Genet , vol.60 , pp. 1251-1256
    • Bidichandani, S.I.1    Ashizawa, T.2    Patel, P.I.3
  • 76
    • 0034192352 scopus 로고    scopus 로고
    • Inactivation of the Friedreich ataxia mouse gene leads to early embryonic lethality without iron accumulation
    • Cossée M, Puccio H, Gansmuller A et al. Inactivation of the Friedreich ataxia mouse gene leads to early embryonic lethality without iron accumulation. Hum Mol Genet 2000; 9:1219-1226.
    • (2000) Hum Mol Genet , vol.9 , pp. 1219-1226
    • Cossée, M.1    Puccio, H.2    Gansmuller, A.3
  • 77
    • 17344377955 scopus 로고    scopus 로고
    • Atypical Friedreich ataxia phenotype associated with a novel missense mutation in the X25 gene
    • De Michele G, Filla A, Cavalcanti F et al. Atypical Friedreich ataxia phenotype associated with a novel missense mutation in the X25 gene. Neurology 2000; 54:496-499.
    • (2000) Neurology , vol.54 , pp. 496-499
    • De Michele, G.1    Filla, A.2    Cavalcanti, F.3
  • 78
    • 0030846021 scopus 로고    scopus 로고
    • Regulation of mitochondrial iron accumulation by YFH1, a putative homolog of frataxin
    • Babcock M, de Silva D, Oaks R et al. Regulation of mitochondrial iron accumulation by YFH1, a putative homolog of frataxin. Science 1997; 276:1709-1712.
    • (1997) Science , vol.276 , pp. 1709-1712
    • Babcock, M.1    De Silva, D.2    Oaks, R.3
  • 79
    • 0033529554 scopus 로고    scopus 로고
    • Yeast and human frataxin are processed to mature form in two sequential steps by the mitochondrial processing peptidase
    • Branda SS, Cavadini P, Adamec J, Kalousek F, Taroni F, Isaya, G. Yeast and human frataxin are processed to mature form in two sequential steps by the mitochondrial processing peptidase. J Biol Chem 1999; 274:22763-22769.
    • (1999) J Biol Chem , vol.274 , pp. 22763-22769
    • Branda, S.S.1    Cavadini, P.2    Adamec, J.3    Kalousek, F.4    Taroni, F.5    Isaya, G.6
  • 81
    • 0032695778 scopus 로고    scopus 로고
    • Maturation of frataxin within mammalian and yeast mitochondria: One-step processing by matrix processing peptidase
    • Gordon DM, Shi Q, Dancis A, Pain D. Maturation of frataxin within mammalian and yeast mitochondria: one-step processing by matrix processing peptidase. Hum Mol Genet 1999; 8:2255-2262.
    • (1999) Hum Mol Genet , vol.8 , pp. 2255-2262
    • Gordon, D.M.1    Shi, Q.2    Dancis, A.3    Pain, D.4
  • 82
    • 0032540929 scopus 로고    scopus 로고
    • Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis
    • Knight SA, Sepuri NB, Pain D, Dancis A. Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis. J Biol Chem 1998; 273:18389-18393.
    • (1998) J Biol Chem , vol.273 , pp. 18389-18393
    • Knight, S.A.1    Sepuri, N.B.2    Pain, D.3    Dancis, A.4
  • 83
    • 0030825723 scopus 로고    scopus 로고
    • Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue
    • Wilson RB, Roof DM. Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue. Nature Genet 1997; 16:352-357.
    • (1997) Nature Genet , vol.16 , pp. 352-357
    • Wilson, R.B.1    Roof, D.M.2
  • 84
    • 0033582421 scopus 로고    scopus 로고
    • The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence for a mitochondrial iron cycle
    • Radisky DC, Babcock MC, Kaplan J. The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence for a mitochondrial iron cycle. J Biol Chem 1999; 274:4497-4499.
    • (1999) J Biol Chem , vol.274 , pp. 4497-4499
    • Radisky, D.C.1    Babcock, M.C.2    Kaplan, J.3
  • 85
    • 0031253821 scopus 로고    scopus 로고
    • Frataxin gene expansion causes aconitase and mitochondrial iron-sulfur protein deficiency in Friedreich ataxia
    • Rötig A, deLonlay P, Chretien D et al. Frataxin gene expansion causes aconitase and mitochondrial iron-sulfur protein deficiency in Friedreich ataxia. Nature Genet 1997; 17:215-217.
    • (1997) Nature Genet , vol.17 , pp. 215-217
    • Rötig, A.1    DeLonlay, P.2    Chretien, D.3
  • 86
    • 0029064257 scopus 로고
    • Superoxide radical and iron modulate aconitase activity in mammalian cells
    • Gardner PR, Rainieri I, Epstein LB, White CW. Superoxide radical and iron modulate aconitase activity in mammalian cells. J Biol Chem 1995; 270:13399-13405.
    • (1995) J Biol Chem , vol.270 , pp. 13399-13405
    • Gardner, P.R.1    Rainieri, I.2    Epstein, L.B.3    White, C.W.4
  • 87
    • 0032746009 scopus 로고    scopus 로고
    • The essential role of mitochondria in the biogenesis of cellular iron-sulfur proteins
    • Lill R, Diekert K, Kaut A et al. The essential role of mitochondria in the biogenesis of cellular iron-sulfur proteins. Biol Chem 1999; 380:1157-1166.
    • (1999) Biol Chem , vol.380 , pp. 1157-1166
    • Lill, R.1    Diekert, K.2    Kaut, A.3
  • 88
    • 0032800601 scopus 로고    scopus 로고
    • Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain
    • Foury F. Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain. FEBS Lett 1999; 456:281-284.
    • (1999) FEBS Lett , vol.456 , pp. 281-284
    • Foury, F.1
  • 89
    • 0002407742 scopus 로고    scopus 로고
    • Frataxin is an iron-storage protein
    • abstract
    • Isaya G, Adamec J, Rusnak F et al. Frataxin is an iron-storage protein. Am J Hum Genet 1999; 65(suppl.):A33 (abstract).
    • (1999) Am J Hum Genet , vol.65 , Issue.SUPPL.
    • Isaya, G.1    Adamec, J.2    Rusnak, F.3
  • 90
    • 0034661480 scopus 로고    scopus 로고
    • Towards a structural understanding of Friedreich's ataxia: The solution structure of frataxin
    • Musco G, Stier G, Kolmerer B, Adinolfi S, Martin S, Frenkiel T et al. Towards a structural understanding of Friedreich's ataxia: The solution structure of frataxin. Structure Fold Des 2000; 8:695-707.
    • (2000) Structure Fold Des , vol.8 , pp. 695-707
    • Musco, G.1    Stier, G.2    Kolmerer, B.3    Adinolfi, S.4    Martin, S.5    Frenkiel, T.6
  • 92
    • 12944257432 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family
    • Cho SJ, Lee MG, Yang JK, Lee JY, Song HK, Suh SW. Crystal structure of Escherichia coli CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family. Proc Natl Acad Sci USA 2000; 97:8932-8937.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8932-8937
    • Cho, S.J.1    Lee, M.G.2    Yang, J.K.3    Lee, J.Y.4    Song, H.K.5    Suh, S.W.6
  • 93
    • 0019169563 scopus 로고
    • The cardiomyopathy of Friedreich ataxia morphological observations in 3 cases
    • Lamarche JB, Côté M, Lemieux B. The cardiomyopathy of Friedreich ataxia morphological observations in 3 cases. Can J Neurol Sci 1980; 7:389-396.
    • (1980) Can J Neurol Sci , vol.7 , pp. 389-396
    • Lamarche, J.B.1    Côté, M.2    Lemieux, B.3
  • 94
    • 0032971328 scopus 로고    scopus 로고
    • Increased iron in the dentate nucleus of patients with Friedreich ataxia
    • Waldvogel D, van Gelderen P, Hallett M. Increased iron in the dentate nucleus of patients with Friedreich ataxia. Ann Neurol 1999; 46:123-125.
    • (1999) Ann Neurol , vol.46 , pp. 123-125
    • Waldvogel, D.1    Van Gelderen, P.2    Hallett, M.3
  • 96
    • 0034642214 scopus 로고    scopus 로고
    • Increased levels of plasma malondialdehyde in Friedreich ataxia
    • Emond M, Lepage G, Vanasse M, Pandolfo M. Increased levels of plasma malondialdehyde in Friedreich ataxia. Neurol 2000; 55:1752-1753.
    • (2000) Neurol , vol.55 , pp. 1752-1753
    • Emond, M.1    Lepage, G.2    Vanasse, M.3    Pandolfo, M.4
  • 97
    • 0033054177 scopus 로고    scopus 로고
    • The Friedreich ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis
    • Wong A, Yang J, Cavadini P, Gellera C, Lonnerdal B, Taroni F, Cortopassi G. The Friedreich ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis. Hum Mol Genet 1999; 8:425-430.
    • (1999) Hum Mol Genet , vol.8 , pp. 425-430
    • Wong, A.1    Yang, J.2    Cavadini, P.3    Gellera, C.4    Lonnerdal, B.5    Taroni, F.6    Cortopassi, G.7
  • 98
    • 0027430101 scopus 로고
    • Friedreich ataxia phenotype not linked to chromosome 9 and associated with selective autosomal recessive vitamin E deficiency in two in-bred Tunisian families
    • Ben Hamida M, Belal S, Sirugo G et al. Friedreich ataxia phenotype not linked to chromosome 9 and associated with selective autosomal recessive vitamin E deficiency in two in-bred Tunisian families. Neurology 1993; 43:2179-2183.
    • (1993) Neurology , vol.43 , pp. 2179-2183
    • Ben Hamida, M.1    Belal, S.2    Sirugo, G.3
  • 99
    • 0026020970 scopus 로고
    • Antioxidant defense systems: The role of carotenoids, tocopherols, and thiols
    • Di Mascio P, Murphy ME, Sies H. Antioxidant defense systems: The role of carotenoids, tocopherols, and thiols. Am J Clin Nutr 1991; 53:194S-200S.
    • (1991) Am J Clin Nutr , vol.53
    • Di Mascio, P.1    Murphy, M.E.2    Sies, H.3
  • 102
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze MW, Kühn LC. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc Natl Acad Sci USA 1996; 93:8175-8182.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kühn, L.C.2
  • 103
    • 0034213821 scopus 로고    scopus 로고
    • Influence of GAA expansion size and disease duration on central nervous system impairment in Friedreich's ataxia: Contribution to the understanding of the pathophysiology of the disease
    • Santoro L, Perretti A, Lanzillo B et al. Influence of GAA expansion size and disease duration on central nervous system impairment in Friedreich's ataxia: contribution to the understanding of the pathophysiology of the disease. Clin Neurophysiol 2000; 111:1023-1030.
    • (2000) Clin Neurophysiol , vol.111 , pp. 1023-1030
    • Santoro, L.1    Perretti, A.2    Lanzillo, B.3
  • 104
    • 0035138072 scopus 로고    scopus 로고
    • Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
    • Puccio H, Simon D, Cossee M, Criqui-Filipe P, Tiziano F, Melki J et al. Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat Genet 2001; 27:181-618.
    • (2001) Nat Genet , vol.27 , pp. 181-618
    • Puccio, H.1    Simon, D.2    Cossee, M.3    Criqui-Filipe, P.4    Tiziano, F.5    Melki, J.6


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